Linked Life Data

12853434

Source:http://linkedlifedata.com/resource/pubmed/id/12853434

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2003-7-10
pubmed:abstractText
The shutoff mechanisms of the rod visual transduction cascade involve G-protein-coupled receptor (GPCR) kinase 1 (GRK1) phosphorylation of light-activated rhodopsin (R*) followed by rod arrestin binding. Deactivation of the cone phototransduction cascade in the mammalian retina is delineated poorly. In this study we sought to explore the potential mechanisms underlying the quenching of the phototransduction cascade in cone photoreceptors by using mouse models lacking rods and/or GRK1. Using the "pure-cone" retinas of the neural retina leucine zipper (Nrl) knock-out (KO, -/-) mice (Mears et al., 2001), we have demonstrated the light-dependent, multi-site phosphorylation of both S and M cone opsins by in situ phosphorylation and isoelectric focusing. Immunoprecipitation with affinity-purified polyclonal antibodies against either mouse cone arrestin (mCAR) or mouse S and M cone opsins revealed specific binding of mCAR to light-activated, phosphorylated cone opsins. To elucidate the potential role of GRK1 in cone opsin phosphorylation, we created Nrl and Grk1 double knock-out (Nrl-/-Grk1-/-) mice by crossing the Nrl-/- mice with Grk1-/- mice (Chen et al., 1999). We found that, in the retina of these mice, the light-activated cone opsins were neither phosphorylated nor bound with mCAR. Our results demonstrate, for the first time in a mammalian species, that cone opsins are phosphorylated and that CAR binds to phosphorylated cone opsins after light activation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1529-2401
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6152-60
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12853434-Animals, pubmed-meshheading:12853434-Arrestin, pubmed-meshheading:12853434-Basic-Leucine Zipper Transcription Factors, pubmed-meshheading:12853434-Cell Membrane, pubmed-meshheading:12853434-DNA-Binding Proteins, pubmed-meshheading:12853434-Darkness, pubmed-meshheading:12853434-Eye Proteins, pubmed-meshheading:12853434-G-Protein-Coupled Receptor Kinase 1, pubmed-meshheading:12853434-Isoelectric Focusing, pubmed-meshheading:12853434-Light, pubmed-meshheading:12853434-Mice, pubmed-meshheading:12853434-Mice, Inbred C57BL, pubmed-meshheading:12853434-Mice, Knockout, pubmed-meshheading:12853434-Phosphorylation, pubmed-meshheading:12853434-Precipitin Tests, pubmed-meshheading:12853434-Protein Binding, pubmed-meshheading:12853434-Protein Kinases, pubmed-meshheading:12853434-Retina, pubmed-meshheading:12853434-Retinal Cone Photoreceptor Cells, pubmed-meshheading:12853434-Rod Opsins, pubmed-meshheading:12853434-Vision, Ocular
pubmed:year
2003
pubmed:articleTitle
GRK1-dependent phosphorylation of S and M opsins and their binding to cone arrestin during cone phototransduction in the mouse retina.
pubmed:affiliation
The Mary D. Allen Laboratory for Vision Research, Doheny Eye Institute, Department of Cell and Neurobiology, the Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9112, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't